Using two different TRAPP subunits as bait, we have identified four additional components of this human vesicle–tethering complex. Functional studies suggest that TRAPP functions early in ER-to-Golgi traffic, at or before the level of the ERGIC compartment.

The TRAPP vesicle-tethering complex consists of more than 10 distinct polypeptides and is involved in protein transport. Using the C2 subunit as bait we identified SPATA4, a spermatocyte-specific protein of unknown function, as an interacting partner in a yeast two hybrid screen. Further studies indicate SPATA4 interacts with the C2 portion of the TRAPP complex. SPATA4 fractionates with both cytosolic and nuclear fractions suggesting it may have several distinct functions. SPATA4 is one of only three human proteins that contain a DUF1042 domain and we show that C2 does not interact with another one of the DUF1042 domain-containing proteins. Our results suggest a role for SPATA4 in membrane traffic and a specialized function for TRAPP in spermatocytes.